1gt7: Difference between revisions

Revision as of 13:53, 21 February 2008

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI

OverviewOverview

The enzyme L-rhamnulose-1-phosphate aldolase catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. It is a homotetramer with an M(r) of 30 000 per subunit and crystallized in space group P3(2)21. The enzyme shows a low sequence identity of 18% with the structurally known L-fuculose-1-phosphate aldolase that splits a stereoisomer in a similar reaction. Structure analysis was initiated with a single heavy-atom derivative measured to 6 A resolution. The resulting poor electron density, a self-rotation function and the working hypothesis that both enzymes are C(4) symmetric with envelopes that resemble one another allowed the location of the 20 protomers of the asymmetric unit. The crystal-packing unit was a D(4)-symmetric propeller consisting of five D(4)-symmetric octamers around an internal crystallographic twofold axis. Presumably, the propellers associate laterally in layers, which in turn pile up along the 3(2) axis to form the crystal. The non-crystallographic symmetry was used to extend the phases to the 2.7 A resolution limit and to establish a refined atomic model of the enzyme. The structure showed that the two enzymes are indeed homologous and that they possess chemically similar active centres.

About this StructureAbout this Structure

1GT7 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Rhamnulose-1-phosphate aldolase, with EC number 4.1.2.19 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging., Kroemer M, Schulz GE, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):824-32. Epub 2002, Apr 26. PMID:11976494

Page seeded by OCA on Thu Feb 21 12:53:40 2008

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OCA

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 ==Overview==
-The enzyme L-rhamnulose-1-phosphate aldolase catalyzes the reversible, cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate and, L-lactaldehyde. It is a homotetramer with an M(r) of 30 000 per subunit, and crystallized in space group P3(2)21. The enzyme shows a low sequence, identity of 18% with the structurally known L-fuculose-1-phosphate, aldolase that splits a stereoisomer in a similar reaction. Structure, analysis was initiated with a single heavy-atom derivative measured to 6 A, resolution. The resulting poor electron density, a self-rotation function, and the working hypothesis that both enzymes are C(4) symmetric with, envelopes that resemble one another allowed the location of the 20, protomers of the asymmetric unit. The crystal-packing unit was a, D(4)-symmetric propeller consisting of five D(4)-symmetric octamers around, an internal crystallographic twofold axis. Presumably, the propellers, associate laterally in layers, which in turn pile up along the 3(2) axis, to form the crystal. The non-crystallographic symmetry was used to extend, the phases to the 2.7 A resolution limit and to establish a refined atomic, model of the enzyme. The structure showed that the two enzymes are indeed, homologous and that they possess chemically similar active centres.
+The enzyme L-rhamnulose-1-phosphate aldolase catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. It is a homotetramer with an M(r) of 30 000 per subunit and crystallized in space group P3(2)21. The enzyme shows a low sequence identity of 18% with the structurally known L-fuculose-1-phosphate aldolase that splits a stereoisomer in a similar reaction. Structure analysis was initiated with a single heavy-atom derivative measured to 6 A resolution. The resulting poor electron density, a self-rotation function and the working hypothesis that both enzymes are C(4) symmetric with envelopes that resemble one another allowed the location of the 20 protomers of the asymmetric unit. The crystal-packing unit was a D(4)-symmetric propeller consisting of five D(4)-symmetric octamers around an internal crystallographic twofold axis. Presumably, the propellers associate laterally in layers, which in turn pile up along the 3(2) axis to form the crystal. The non-crystallographic symmetry was used to extend the phases to the 2.7 A resolution limit and to establish a refined atomic model of the enzyme. The structure showed that the two enzymes are indeed homologous and that they possess chemically similar active centres.
 ==About this Structure==
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 [[Category: Single protein]]
 [[Category: Kroemer, M.]]
-[[Category: Schulz, G.E.]]
+[[Category: Schulz, G E.]]
 [[Category: PGH]]
 [[Category: ZN]]
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 [[Category: zinc enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:42:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:40 2008''